登録情報 データベース : EMDB / ID : EMD-30199 構造の表示 ダウンロードとリンクタイトル Cryo-EM reconstruction of PEGylated full-length NOD2 マップデータ 詳細 試料複合体 : NOD2 complexed with ADP 詳細機能・相同性 機能・相同性情報分子機能 ドメイン・相同性 構成要素
detection of muramyl dipeptide / muramyl dipeptide binding / host-mediated modulation of intestinal microbiota composition / regulation of appetite / intestinal stem cell homeostasis / maintenance of gastrointestinal epithelium / positive regulation of mitophagy / antibacterial innate immune response / positive regulation of B cell activation / positive regulation of protein K63-linked ubiquitination ... detection of muramyl dipeptide / muramyl dipeptide binding / host-mediated modulation of intestinal microbiota composition / regulation of appetite / intestinal stem cell homeostasis / maintenance of gastrointestinal epithelium / positive regulation of mitophagy / antibacterial innate immune response / positive regulation of B cell activation / positive regulation of protein K63-linked ubiquitination / cellular response to muramyl dipeptide / positive regulation of stress-activated MAPK cascade / positive regulation of type 2 immune response / CARD domain binding / positive regulation of cytokine production involved in immune response / peptidoglycan binding / nucleotide-binding oligomerization domain containing 2 signaling pathway / positive regulation of cytokine production involved in inflammatory response / extrinsic component of plasma membrane / temperature homeostasis / pattern recognition receptor activity / positive regulation of interleukin-17 production / response to muramyl dipeptide / canonical NF-kappaB signal transduction / detection of bacterium / phagocytic vesicle / Hsp70 protein binding / ubiquitin binding / positive regulation of interleukin-1 beta production / positive regulation of interleukin-8 production / positive regulation of JNK cascade / Hsp90 protein binding / positive regulation of non-canonical NF-kappaB signal transduction / ADP binding / autophagy / positive regulation of interleukin-6 production / positive regulation of tumor necrosis factor production / actin binding / cellular response to lipopolysaccharide / regulation of inflammatory response / regulation of apoptotic process / basolateral plasma membrane / adaptive immune response / cytoskeleton / positive regulation of canonical NF-kappaB signal transduction / defense response to bacterium / protein kinase binding / protein-containing complex binding / cell surface / Golgi apparatus / positive regulation of transcription by RNA polymerase II / protein-containing complex / mitochondrion / ATP binding / cytosol 類似検索 - 分子機能 : / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 / NOD2, winged helix domain / NOD2 winged helix domain / NACHT nucleoside triphosphatase / NACHT domain / NACHT-NTPase domain profile. / Leucine rich repeat, ribonuclease inhibitor type / Leucine Rich repeat ... : / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 / NOD2, winged helix domain / NOD2 winged helix domain / NACHT nucleoside triphosphatase / NACHT domain / NACHT-NTPase domain profile. / Leucine rich repeat, ribonuclease inhibitor type / Leucine Rich repeat / CARD domain / CARD caspase recruitment domain profile. / Caspase recruitment domain / Death-like domain superfamily / Leucine-rich repeat profile. / Leucine-rich repeat / Leucine-rich repeat domain superfamily / P-loop containing nucleoside triphosphate hydrolase 類似検索 - ドメイン・相同性 Nucleotide-binding oligomerization domain-containing protein 2 類似検索 - 構成要素生物種 Oryctolagus cuniculus (ウサギ)手法 単粒子再構成法 / クライオ電子顕微鏡法 / 解像度 : 3.7 Å 詳細 データ登録者Zhang Z / Ohto U / Shimizu T 引用ジャーナル : Structure / 年 : 2021タイトル : Improving particle quality in cryo-EM analysis using a PEGylation method.著者 : Zhikuan Zhang / Hideki Shigematsu / Toshiyuki Shimizu / Umeharu Ohto / 要旨 : Cryo-electron microscopy (cryo-EM) is widely used for structural biology studies and has been developed extensively in recent years. However, its sample vitrification process is a major limitation ... Cryo-electron microscopy (cryo-EM) is widely used for structural biology studies and has been developed extensively in recent years. However, its sample vitrification process is a major limitation because it causes severe particle aggregation and/or denaturation. This effect is thought to occur because particles tend to stick to the "deadly" air-water interface during vitrification. Here, we report a method for PEGylation of proteins that can efficiently protect particles against such problems during vitrification. This method alleviates the laborious process of fine-tuning the vitrification conditions, allowing for analysis of samples that would otherwise be discarded. 履歴 登録 2020年4月8日 - ヘッダ(付随情報) 公開 2021年6月16日 - マップ公開 2021年6月16日 - 更新 2021年10月20日 - 現状 2021年10月20日 処理サイト : PDBj / 状態 : 公開
すべて表示 表示を減らす